Abstract

A fundamental question in biology is how different signaling pathways use common signaling proteins to attain different developmental outcomes. The yeast transcription factor Ste12 is required in at least two distinct signaling processes, each regulated by many of the same protein kinases. Whereas Ste12-Ste12 homodimers promote transcription of genes required for mating, Ste12-Tec1 heterodimers activate genes required for invasive growth. We report that Ste12 and Tec1 undergo covalent modification by the ubiquitin-related modifier SUMO. Stimulation by mating pheromone promotes sumoylation of Ste12 and diminishes the sumoylation of Tec1. In the absence of sumoylation Tec1 is more rapidly degraded. We propose that pheromone-regulated sumoylation of Ste12 and Tec1 promotes a developmental switch from the invasive to the mating differentiation program.

Highlights

  • Fus3 and Kss1 are mitogen-activated protein (MAP)2 kinases that phosphorylate substrates required for signaling in both the mating and invasive growth pathways

  • Phosphorylation of Ste12 promotes binding to a specific DNA sequence called the pheromone-response element (PRE) [3,4,5,6], where it initiates transcription of genes required for efficient mating [7,8,9]

  • Stimulation by mating pheromone promotes sumoylation of Ste12, the same treatment inhibits sumoylation of Tec1 and the protein is instead degraded. These findings suggest that pheromone-regulated sumoylation of transcription factors underlies the developmental switch from the invasive to the mating differentiation program

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Summary

Introduction

Fus3 and Kss1 are mitogen-activated protein (MAP)2 kinases that phosphorylate substrates required for signaling in both the mating and invasive growth pathways. Phosphorylation of Ste12 promotes binding to a specific DNA sequence called the pheromone-response element (PRE) [3,4,5,6], where it initiates transcription of genes required for efficient mating [7,8,9]. Stimulation by mating pheromone promotes sumoylation of Ste12, the same treatment inhibits sumoylation of Tec1 and the protein is instead degraded.

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